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Volumn 51, Issue 2, 2017, Pages 288-294

D-tagatose production by Lactococcus lactis NZ9000 cells harboring Lactobacillus plantarum L-arabinose isomerase

Author keywords

D tagatose; Galactose; L arabinose isomerase; Lactobacillus plantarum; Lactococcus lactis NZ9000

Indexed keywords

ARABINOSE ISOMERASE; GALACTOSE; ISOMERASE; MANGANESE; TAGATOSE; UNCLASSIFIED DRUG;

EID: 85017172130     PISSN: 00195464     EISSN: None     Source Type: Journal    
DOI: 10.5530/ijper.51.2.34     Document Type: Article
Times cited : (7)

References (29)
  • 1
    • 0004670514 scopus 로고
    • Composition of the gum of Sterculia setigera; occurrence of D-tagatose in nature
    • Hirst E L, Hough L, Jones J K. Composition of the gum of Sterculia setigera; occurrence of D-tagatose in nature. Nature. 1949;163(4135):177-82. https://doi.org/10.1038/163177b0 PMid:18213788.
    • (1949) Nature , vol.163 , Issue.4135 , pp. 177-182
    • Hirst, E.L.1    Hough, L.2    Jones, J.K.3
  • 2
    • 84867719252 scopus 로고    scopus 로고
    • Characterization of Moringa oleifera Lam. Gum to establish it as a pharmaceutical excipient
    • Jarald E E, Sharma S, Sheeja E, Ahmad S, Patni S, Daud A. Characterization of Moringa oleifera Lam. gum to establish it as a pharmaceutical excipient. Indian J Pharm Educ Res. 2012;46(3):211-6.
    • (2012) Indian J Pharm Educ Res , vol.46 , Issue.3 , pp. 211-216
    • Jarald, E.E.1    Sharma, S.2    Sheeja, E.3    Ahmad, S.4    Patni, S.5    Daud, A.6
  • 3
    • 0023337855 scopus 로고
    • Effect of the protein, citrate and phosphate content of milk on formation of lactulose during heat treatment
    • Andrews G R, Prasad S K. Effect of the protein, citrate and phosphate content of milk on formation of lactulose during heat treatment. J Dairy Res. 1987;54(2):207-18. https://doi.org/10.1017/S0022029900025358.
    • (1987) J Dairy Res , vol.54 , Issue.2 , pp. 207-218
    • Andrews, G.R.1    Prasad, S.K.2
  • 4
    • 0028839816 scopus 로고
    • Sugar substitutes: Their energy values, bulk characteristics, and potential health benefits
    • Levin G V, Zehner L R, Saunders J P, Beadle J R. Sugar substitutes: their energy values, bulk characteristics, and potential health benefits. Am J Clin Nutr. 1995;62(5):1161-8.
    • (1995) Am J Clin Nutr , vol.62 , Issue.5 , pp. 1161-1168
    • Levin, G.V.1    Zehner, L.R.2    Saunders, J.P.3    Beadle, J.R.4
  • 5
    • 17144375651 scopus 로고    scopus 로고
    • Chemical indicators of heat treatment in fortified and special milks
    • Mendoza M R, Olano A, Villamiel M. Chemical indicators of heat treatment in fortified and special milks. J Agric Food Chem. 2005;53(8):2995-9. https://doi.org/10.1021/jf040406l PMid:15826050.
    • (2005) J Agric Food Chem , vol.53 , Issue.8 , pp. 2995-2999
    • Mendoza, M.R.1    Olano, A.2    Villamiel, M.3
  • 6
    • 4544346270 scopus 로고    scopus 로고
    • Current studies on biological tagatose production using L-arabinose isomerase: A review and future perspective
    • Kim P. Current studies on biological tagatose production using L-arabinose isomerase: a review and future perspective. Appl Microbiol Biotechnol. 2004;65(3):243-9. https://doi.org/10.1007/s00253-004-1665-8 PMid:15248040.
    • (2004) Appl Microbiol Biotechnol , vol.65 , Issue.3 , pp. 243-249
    • Kim, P.1
  • 7
    • 38049186809 scopus 로고    scopus 로고
    • Tagatose, a new antidiabetic and obesity control drug
    • Lu Y, Levin G V, Donner T W. Tagatose, a new antidiabetic and obesity control drug. Diabetes Obes Metab. 2008;10(2):109-34. PMid:17941870.
    • (2008) Diabetes Obes Metab , vol.10 , Issue.2 , pp. 109-134
    • Lu, Y.1    Levin, G.V.2    Donner, T.W.3
  • 8
    • 85017118079 scopus 로고    scopus 로고
    • Dumping for type-2 diabetes
    • Mason E E. Dumping for type-2 diabetes. J Obes Metab Res. 2015;2(1):3-4. https://doi.org/10.4103/2347-9906.148593.
    • (2015) J Obes Metab Res , vol.2 , Issue.1 , pp. 3-4
    • Mason, E.E.1
  • 9
    • 85017107752 scopus 로고    scopus 로고
    • Fighting cancer through an informed society
    • Mehta P, Bhajoni P S, Mehta S P. Fighting cancer through an informed society. JOSH-Diabetes. 2016;4(2):57-66. https://doi.org/10.4103/2321-0656.187996.
    • (2016) Josh-Diabetes , vol.4 , Issue.2 , pp. 57-66
    • Mehta, P.1    Bhajoni, P.S.2    Mehta, S.P.3
  • 12
    • 84865504323 scopus 로고    scopus 로고
    • Sugar substitutes: Health controversy over perceived benefits
    • Tandel K R. Sugar substitutes: Health controversy over perceived benefits. J Pharmacol Pharmacother. 2011;2(4):236-43. https://doi.org/10.4103/0976-500X.85936 PMCid:PMC3198517.
    • (2011) J Pharmacol Pharmacother , vol.2 , Issue.4 , pp. 236-243
    • Tandel, K.R.1
  • 14
    • 34547600568 scopus 로고    scopus 로고
    • Tagatose: Properties, applications, and biotechnological processes
    • Oh D K. Tagatose: properties, applications, and biotechnological processes. Appl Microbiol Biotechnol. 2007;76(1):1-8. https://doi.org/10.1007/s00253-007-0981-1 PMid:17492284.
    • (2007) Appl Microbiol Biotechnol , vol.76 , Issue.1 , pp. 1-8
    • Oh, D.K.1
  • 15
    • 0027551680 scopus 로고
    • Bioconversion of D-galactose into D-tagatose
    • Cheetham P S J, Wootton AN. Bioconversion of D-galactose into D-tagatose. Enzyme Microb Technol. 1993;15(2):105-8. https://doi.org/10.1016/0141-0229(93)90032-W.
    • (1993) Enzyme Microb Technol , vol.15 , Issue.2 , pp. 105-108
    • Cheetham, P.S.J.1    Wootton, A.N.2
  • 16
    • 0037357583 scopus 로고    scopus 로고
    • A feasible enzymatic process for D-tagatose production by an immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor
    • Kim H J, Ryu S A, Kim P, Oh D K. A feasible enzymatic process for D-tagatose production by an immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor. Biotechnol Prog. 2003;19(2):400-4. https://doi. org/10.1021/bp025675f.
    • (2003) Biotechnol Prog , vol.19 , Issue.2 , pp. 400-404
    • Kim, H.J.1    Ryu, S.A.2    Kim, P.3    Oh, D.K.4
  • 17
    • 84872155756 scopus 로고    scopus 로고
    • Prebiotics, probiotics and synbiotics: An overview
    • Sekhon B S, Jairath S. Prebiotics, probiotics and synbiotics: an overview. Indian J Pharm Educ Res. 2010;1(2):13-8.
    • (2010) Indian J Pharm Educ Res , vol.1 , Issue.2 , pp. 13-18
    • Sekhon, B.S.1    Jairath, S.2
  • 18
    • 0037299866 scopus 로고    scopus 로고
    • Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production
    • Yoon S H, Kim P, Oh D K. Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production. World J Microbiol Biotechnol. 2003;19(1):47-51. https://doi.org/10.1023/A:1022575601492.
    • (2003) World J Microbiol Biotechnol , vol.19 , Issue.1 , pp. 47-51
    • Yoon, S.H.1    Kim, P.2    Oh, D.K.3
  • 19
    • 36348972810 scopus 로고    scopus 로고
    • Characterization of an L-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH
    • Chouayekh H, Bejar W, Rhimi M K Mseddi, Bejar S. Characterization of an L-arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH. FEMS Microbiol Lett. 2007;277(2):260-7. https://doi.org/10.1111/j.1574-6968.2007.00961.x PMid:18031349.
    • (2007) FEMS Microbiol Lett , vol.277 , Issue.2 , pp. 260-267
    • Chouayekh, H.1    Bejar, W.2    Rhimi, M.K.3    Mseddibejar, S.4
  • 20
    • 85017139643 scopus 로고    scopus 로고
    • Partially purified exopolysaccharide from Lactobacillus plantarum YML009 with total phenolic content, antioxidant and free radical scavenging efficacy
    • Seo B J, Bajpai V K, Rather I A, Park Y H. Partially purified exopolysaccharide from Lactobacillus plantarum YML009 with total phenolic content, antioxidant and free radical scavenging efficacy. Indian J Pharm Educ Res. 2015;49(4):282-92. https://doi.org/10.5530/ijper.49.4.6.
    • (2015) Indian J Pharm Educ Res , vol.49 , Issue.4 , pp. 282-292
    • Seo, B.J.1    Bajpai, V.K.2    Rather, I.A.3    Park, Y.H.4
  • 21
    • 79952814999 scopus 로고    scopus 로고
    • A novel L-arabinose isomerase from Lactobacillus fermentum CGMCC2921 for D-tagatose production: Gene cloning, purification and characterization
    • Xu Z, Qing L, Y Li, Feng X, Xu H, Ouyang P. A novel L-arabinose isomerase from Lactobacillus fermentum CGMCC2921 for D-tagatose production: Gene cloning, purification and characterization. J Mol Catal B Enzym. 2011;70(1):1-7. https://doi.org/10.1016/j.molcatb.2011.01.010.
    • (2011) J Mol Catal B Enzym , vol.70 , pp. 1-7
    • Xu, Z.1    Qing, L.2    Li, Y.3    Feng, X.4    Xu, H.5    Ouyang, P.6
  • 22
    • 84865272522 scopus 로고    scopus 로고
    • A method for the production of D-tagatose using a recombinant Pichiapastoris strain secreting β-D-galactosidase from Arthrobacter chlorophenolicus and a recombinant L-arabinose isomerase from Arthrobacter
    • Wanarska M, Kur J. A method for the production of D-tagatose using a recombinant Pichiapastoris strain secreting β-D-galactosidase from Arthrobacter chlorophenolicus and a recombinant L-arabinose isomerase from Arthrobacter. Microb Cell Fact. 2012;11(1):1-15. https://doi. org/10.1186/1475-2859-11-113 PMid:22917022 PMCid:PMC3520711.
    • (2012) Microb Cell Fact , vol.11 , Issue.1 , pp. 1-15
    • Wanarska, M.1    Kur, J.2
  • 23
    • 77955665578 scopus 로고    scopus 로고
    • The acid tolerant L-arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive D-tagatose producer
    • Rhimi M, Ilhammami R, Bajic G, Boudebbouze S, Maguin E, Haser R, Aghajari N. The acid tolerant L-arabinose isomerase from the food grade Lactobacillus sakei 23K is an attractive D-tagatose producer. Bioresour Technol. 2010;101(23):9171-7. https://doi.org/10.1016/j.biortech.2010.07.036 PMid:20688514.
    • (2010) Bioresour Technol , vol.101 , Issue.23 , pp. 9171-9177
    • Rhimi, M.1    Ilhammami, R.2    Bajic, G.3    Boudebbouze, S.4    Maguin, E.5    Haser, R.6    Aghajari, N.7
  • 24
    • 84866740969 scopus 로고    scopus 로고
    • Bifidobacterium longum L-arabinose isomerase-overexpression in Lactococcus lactis, purification, and characterization
    • Salonen N, Nyyssölä A, Salonen K, Turunen O. Bifidobacterium longum L-arabinose isomerase-overexpression in Lactococcus lactis, purification, and characterization. Appl Biochem Biotechnol. 2012;168(2):392-405. https://doi.org/10.1007/s12010-012-9783-8 PMid:22763951.
    • (2012) Appl Biochem Biotechnol , vol.168 , Issue.2 , pp. 392-405
    • Salonen, N.1    Nyyssölä, A.2    Salonen, K.3    Turunen, O.4
  • 25
    • 0037742418 scopus 로고    scopus 로고
    • Production of tagatose by a recombinant thermostable L-arabinose isomerase from Thermus sp
    • Kim J W, Roh H J, Kim HY, Cha JH et al. Production of tagatose by a recombinant thermostable L-arabinose isomerase from Thermus sp. Biotechnol Lett. 2003;25(12):963-67. https://doi.org/10.1023/A:1024069813839 PMid:12889832.
    • (2003) Biotechnol Lett , vol.25 , Issue.12 , pp. 963-967
    • Kim, J.W.1    Roh, H.J.2    Kim, H.Y.3    Cha, J.H.4
  • 26
    • 84880136941 scopus 로고    scopus 로고
    • D-Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum L-arabinose isomerase
    • Salonen N, Salonen K, Leisola M, Nyyssölä A. D-Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum L-arabinose isomerase. Bioprocess Biosyst Eng. 2012;36(4):489-97. https://doi.org/10.1007/s00449-012-0805-2.
    • (2012) Bioprocess Biosyst Eng , vol.36 , Issue.4 , pp. 489-497
    • Salonen, N.1    Salonen, K.2    Leisola, M.3    Nyyssölä, A.4
  • 27
    • 0036727268 scopus 로고    scopus 로고
    • In situ determination of the intracellular pH of Lactococcus lactis and Lactobacillus plantarum during pressure treatment
    • Molinagutierrez A, Stippl V, Delgado A, Gänzle M G, Vogel R F. In situ determination of the intracellular pH of Lactococcus lactis and Lactobacillus plantarum during pressure treatment. Appl Environ Microbiol. 2002;68(9):4399-406. https://doi.org/10.1128/AEM.68.9.4399-4406.2002 PMCid:PMC124068.
    • (2002) Appl Environ Microbiol , vol.68 , Issue.9 , pp. 4399-4406
    • Molinagutierrez, A.1    Stippl, V.2    Delgado, A.3    Gänzle, M.G.4    Vogel, R.F.5
  • 28
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • De Ruyter P G, Kuipers O P, De Vos W M. Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl Environ Microbiol. 1996;62(10):3662-7. PMid:8837421 PMCid:PMC168174.
    • (1996) Appl Environ Microbiol , vol.62 , Issue.10 , pp. 3662-3667
    • De Ruyter, P.G.1    Kuipers, O.P.2    De Vos, W.M.3
  • 29
    • 0345471372 scopus 로고    scopus 로고
    • Quorum sensing-controlled gene expression in lactic acid bacteria
    • Kuipers O, Oscar P. Quorum sensing-controlled gene expression in lactic acid bacteria. J Biotechnol. 1998;64(1):15-21. https://doi.org/10.1016/S0168-1656(98)00100-X.
    • (1998) J Biotechnol , vol.64 , Issue.1 , pp. 15-21
    • Kuipers, O.1    Oscar, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.